Alina Negoi

Sn‐Doped Hydroxylated MgF2 Catalysts for the Fast and Selective Saccharification of Cellulose to Glucose

TIN, TAILORED, NOT SOLDER, BUT CAT: Doped hydroxylated fluorides, prepared by a modified sol-gel method, offer enhanced acidity and improved stability against water, and efficiency in the degradation of cellulose. These materials extend the portfolio of acid catalysts for fast and selective hydrolysis of biomass to glucose, which offers a feedstock for bioethanol production.

Direct synthesis of sorbitol and glycerol from cellulose over ionic Ru/magnetite nanoparticles in the absence of external hydrogen.

A sweet catalyst: A catalyst formed of Ru/functionalized silica-coated magnetite nanoparticles is highly efficient in the one-pot production of sorbitol and glycerol, starting from cellulose and in the absence of an external hydrogen source. The ease of recoverability of the catalyst from the solid residues, and its reuse without loss of activity or selectivity for several runs, is an important green element of the process.

Bifunctional carbohydrate biopolymers entrapped lipase as catalyst for the two consecutive conversions of α-pinene to oxy-derivatives.

Bifunctional catalysts designed as carbohydrate biopolymers entrapping lipase have been investigated for the biotransformation of a natural compound (α-pinene) to oxy-derivatives. Lipases assisted the epoxidation of α-pinene using H2O2 as oxidation reagent and ethyl acetate as both acetate-supplier and solvent affording α-pinene oxide as the main product. Further, the biopolymer promoted the isomerization of α-pinene oxide to campholenic aldehyde and trans-carenol. In this case, the biopolymers played double roles of the support and also active part of the bifunctional catalyst. Screening of enzymes and their entrapping in a biopolymeric matrix (e.g. Ca-alginate and κ-carrageenan) indicated the lipase extracted from Aspergillus niger as the most efficient. In addition, the presence of biopolymers enhanced the catalytic activity of the immobilized lipase (i.e. 13.39×10(3), 19.76×10(3)and 26.46×10(3) for the free lipase, lipase-carrageenan and lipase-alginate, respectively). The catalysts stability and reusability were confirmed in eight consecutively reaction runs.